Characterization and inhibition of norovirus proteases of genogroups I and II using a fluorescence resonance energy transfer assay

Kyeong Ok Chang, Daisuke Takahashi, Om Prakash, Yunjeong Kim

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Noroviruses are the major cause of food- or water-borne gastroenteritis outbreaks in humans. The norovirus protease that cleaves a large viral polyprotein to nonstructural proteins is essential for virus replication and an attractive target for antiviral drug development. Noroviruses show high genetic diversity with at least five genogroups, GI-GV, of which GI and GII are responsible for the majority of norovirus infections in humans. We cloned and expressed proteases of Norwalk virus (GI) and MD145 virus (GII) and characterized the enzymatic activities with fluorescence resonance energy transfer substrates. We demonstrated that the GI and GII proteases cleaved the substrates derived from the naturally occurring cleavage site in the open reading frame (ORF) 1 of G1 norovirus with similar efficiency, and that enzymatic activity of both proteases was inhibited by commercial protease inhibitors including chymostatin. The interaction of chymostatin to Norwalk virus protease was validated by nuclear magnetic resonance (NMR) spectroscopy.

Original languageEnglish
Pages (from-to)125-133
Number of pages9
JournalVirology
Volume423
Issue number2
DOIs
Publication statusPublished - Feb 20 2012

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Norovirus
Fluorescence Resonance Energy Transfer
Peptide Hydrolases
Genotype
Norwalk virus
Polyproteins
Gastroenteritis
Virus Replication
Protease Inhibitors
Open Reading Frames
Antiviral Agents
Disease Outbreaks
Magnetic Resonance Spectroscopy
Viruses
Food
Water
Infection
Proteins

All Science Journal Classification (ASJC) codes

  • Virology

Cite this

Characterization and inhibition of norovirus proteases of genogroups I and II using a fluorescence resonance energy transfer assay. / Chang, Kyeong Ok; Takahashi, Daisuke; Prakash, Om; Kim, Yunjeong.

In: Virology, Vol. 423, No. 2, 20.02.2012, p. 125-133.

Research output: Contribution to journalArticle

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